Polyvalent anti-immunoglobulins, an anti fab, and class-specific anti IgM, anti gamma, anti gamma 2, and anti IgA were purified by affinity chromatography on columns of myeloma proteins covalently coupled to sepharose. Purified anti immunoglobulin was covalently coupled to Sephadex G-200, and lymphoid cells were fractionated on columns thus prepared. Most of the immunoglobulin bearing lymphocytes adhered to the columns and could be eluted with soluble myeloma proteins or normal immunoglobulin. Most of the thymus derived cells passed through the columns. These columns provide a means of specifically separating T- lymphocytes and B-lymphocytes.